BAIT
RHBDD1
RRP4, HSD50
rhomboid domain containing 1
GO Process (12)
GO Function (3)
GO Component (3)
Gene Ontology Biological Process
- ER-associated ubiquitin-dependent protein catabolic process [ISS]
- cellular response to UV [ISS]
- cellular response to unfolded protein [ISS]
- membrane protein intracellular domain proteolysis [ISS]
- membrane protein proteolysis [IDA]
- negative regulation of apoptotic process [IDA, IMP, ISS]
- positive regulation of protein catabolic process [IDA, IMP]
- positive regulation of protein processing [ISS]
- positive regulation of secretion [IMP]
- post-translational protein modification [ISS]
- regulation of male germ cell proliferation [ISS]
- spermatid differentiation [ISS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
VAMP3
CEB
vesicle-associated membrane protein 3
GO Process (14)
GO Function (3)
GO Component (8)
Gene Ontology Biological Process
- exocytosis [TAS]
- membrane fusion [TAS]
- mucus secretion [IMP]
- negative regulation of secretion by cell [IDA]
- neurotransmitter secretion [IBA]
- positive regulation of immunoglobulin secretion [IMP]
- positive regulation of receptor recycling [ISS]
- protein complex assembly [TAS]
- regulation of histamine secretion by mast cell [IMP]
- retrograde transport, endosome to Golgi [IDA]
- substrate adhesion-dependent cell spreading [ISS]
- vesicle docking involved in exocytosis [TAS]
- vesicle fusion [IBA]
- vesicle-mediated transport [ISS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
Proximity Label-MS
An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.
Publication
Spatial proteomics reveal that the protein phosphatase PTP1B interacts with and may modify tyrosine phosphorylation of the rhomboid protease RHBDL4.
Rhomboid-like proteins are evolutionarily conserved, ubiquitous polytopic membrane proteins, including the canonical rhomboid intramembrane serine proteases and also others that have lost protease activity during evolution. We still have much to learn about their cellular roles, and evidence suggests that some may have more than one function. For example, RHBDL4 (rhomboid-like protein 4) is an endoplasmic reticulum (ER)-resident protease that ... [more]
J. Biol. Chem. Dec. 26, 2018; 294(30);11486-11497 [Pubmed: 31177093]
Throughput
- High Throughput
Curated By
- BioGRID